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Database: UniProt
Entry: R5HAG8_9FIRM
LinkDB: R5HAG8_9FIRM
Original site: R5HAG8_9FIRM 
ID   R5HAG8_9FIRM            Unreviewed;       363 AA.
AC   R5HAG8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   RecName: Full=Riboflavin biosynthesis protein RibD {ECO:0000256|PIRNR:PIRNR006769};
DE   Includes:
DE     RecName: Full=Diaminohydroxyphosphoribosylaminopyrimidine deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE              Short=DRAP deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE              EC=3.5.4.26 {ECO:0000256|PIRNR:PIRNR006769};
DE     AltName: Full=Riboflavin-specific deaminase {ECO:0000256|PIRNR:PIRNR006769};
DE   Includes:
DE     RecName: Full=5-amino-6-(5-phosphoribosylamino)uracil reductase {ECO:0000256|PIRNR:PIRNR006769};
DE              EC=1.1.1.193 {ECO:0000256|PIRNR:PIRNR006769};
DE     AltName: Full=HTP reductase {ECO:0000256|PIRNR:PIRNR006769};
GN   ORFNames=BN469_01392 {ECO:0000313|EMBL:CCY26493.1};
OS   Firmicutes bacterium CAG:114.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263001 {ECO:0000313|EMBL:CCY26493.1, ECO:0000313|Proteomes:UP000018090};
RN   [1] {ECO:0000313|EMBL:CCY26493.1, ECO:0000313|Proteomes:UP000018090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:114 {ECO:0000313|Proteomes:UP000018090};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-
CC       phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-
CC       phosphate. {ECO:0000256|ARBA:ARBA00002151,
CC       ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine +
CC         H(+) + H2O = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+);
CC         Xref=Rhea:RHEA:21868, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:58453, ChEBI:CHEBI:58614; EC=3.5.4.26;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-
CC         amino-6-(5-phospho-D-ribosylamino)uracil + H(+) + NADPH;
CC         Xref=Rhea:RHEA:17845, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, ChEBI:CHEBI:58421, ChEBI:CHEBI:58453;
CC         EC=1.1.1.193; Evidence={ECO:0000256|PIRNR:PIRNR006769};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRNR:PIRNR006769,
CC         ECO:0000256|PIRSR:PIRSR006769-3};
CC       Note=Binds 1 zinc ion. {ECO:0000256|PIRNR:PIRNR006769,
CC       ECO:0000256|PIRSR:PIRSR006769-3};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 2/4. {ECO:0000256|ARBA:ARBA00004882,
CC       ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-
CC       ribitylamino)uracil from GTP: step 3/4. {ECO:0000256|ARBA:ARBA00004910,
CC       ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the HTP reductase
CC       family. {ECO:0000256|ARBA:ARBA00007417, ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the cytidine and
CC       deoxycytidylate deaminase family. {ECO:0000256|ARBA:ARBA00005259,
CC       ECO:0000256|PIRNR:PIRNR006769}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCY26493.1}.
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DR   EMBL; CAXW010000106; CCY26493.1; -; Genomic_DNA.
DR   AlphaFoldDB; R5HAG8; -.
DR   STRING; 1263001.BN469_01392; -.
DR   UniPathway; UPA00275; UER00401.
DR   Proteomes; UP000018090; Unassembled WGS sequence.
DR   GO; GO:0008703; F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008835; F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd01284; Riboflavin_deaminase-reductase; 1.
DR   Gene3D; 3.40.140.10; Cytidine Deaminase, domain 2; 1.
DR   Gene3D; 3.40.430.10; Dihydrofolate Reductase, subunit A; 1.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   InterPro; IPR024072; DHFR-like_dom_sf.
DR   InterPro; IPR004794; Eubact_RibD.
DR   InterPro; IPR011549; RibD_C.
DR   InterPro; IPR002734; RibDG_C.
DR   NCBIfam; TIGR00326; eubact_ribD; 1.
DR   NCBIfam; TIGR00227; ribD_Cterm; 1.
DR   PANTHER; PTHR38011:SF7; 2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE; 1.
DR   PANTHER; PTHR38011; DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820); 1.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   Pfam; PF01872; RibD_C; 1.
DR   PIRSF; PIRSF006769; RibD; 1.
DR   SUPFAM; SSF53927; Cytidine deaminase-like; 1.
DR   SUPFAM; SSF53597; Dihydrofolate reductase-like; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006769};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR006769};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|PIRNR:PIRNR006769};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR006769};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018090};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|PIRNR:PIRNR006769};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRNR:PIRNR006769}.
FT   DOMAIN          1..123
FT                   /note="CMP/dCMP-type deaminase"
FT                   /evidence="ECO:0000259|PROSITE:PS51747"
FT   ACT_SITE        52
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-1"
FT   BINDING         50
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT   BINDING         75
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT   BINDING         84
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-3"
FT   BINDING         154
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         168
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         170
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         196
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         200
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         207
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         221
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
FT   BINDING         295..301
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006769-2"
SQ   SEQUENCE   363 AA;  38419 MW;  702B3428391282F1 CRC64;
     MTDQDYMALA LDLAQKGAGW TSPNPMVGAV LVKQGRIIGQ GYHARWGDLH AERAALAACR
     EDPAGSTLYV TLEPCCHQGK QPPCTQAILE AGITRVVVGS GDPNPLVAGQ GLAQLRAQGV
     QVTEGVLAEE CRALNHVFFH YIQTGRPYVV LKYAMTLDGK LAAYTGASQW ITGEAARRHV
     HTQRGRYRSI LVGVGTVLAD DPQLTCRMEG GRNPLRLVCD THLRTPLTAQ VVKTAGEVPT
     CLATCVTQEG RLAPYRDLGV QILPLPQGAD GHVDLAALVT LLGKMGVDSV LAEGGAQLHW
     GLVQAGLVNR VQAYLAPKLL GGQGAKSPVG GQGFPHPDQA LSLSSPTLTR LGEDILLESE
     VTG
//
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